ArticleInternational journal of molecular sciences2025
Various Options for Covalent Immobilization of Cysteine Proteases-Ficin, Papain, Bromelain.
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Bovine Serum Albumin-Trypsin Sponges for Enhanced Enzymatic Stability and Protein Digestion Efficiency.ACS applied bio materials · 2025Article
- Prospects and problems in enzyme immobilization methodology: comprehensive review.Biophysical reviews · 2025Review
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3 authors.
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Abstract
This study explores various methods for the covalent immobilization of cysteine proteases (ficin, papain, and bromelain). Covalent immobilization involves the formation of covalent bonds between the enzyme and a carrier or between enzyme molecules themselves without a carrier using a crosslinking agent. This process enhances the stability of the enzyme and allows for the creation of preparations with specific and controlled properties. The objective of this study is to evaluate the impact of covalent immobilization under different conditions on the proteolytic activity of the enzymes. The most favorable results were achieved by immobilizing ficin and bromelain through covalent bonding to medium and high molecular weight chitosans, using 5 and 3.33% glutaraldehyde solutions, respectively. For papain, 5 and 6.67% glutaraldehyde solutions proved to be more effective as crosslinking agents. These findings indicate that covalent immobilization can enhance the performance of these enzymes as biocatalysts, with potential applications in various biotechnological fields.
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